Sequence variation of Vanabin2-like vanadium-binding proteins in blood cells of the vanadium-accumulating ascidian Ascidia sydneiensis samea
Use this link to cite this item : https://ir.lib.hiroshima-u.ac.jp/00025974
ID | 25974 |
file | |
creator |
Satake, Makoto
Kamino, Kei
Michibata, Hitoshi
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subject | vanadium
ascidian
metal binding protein
gene expression
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NDC |
Biology
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abstract | The blood cells of ascidians accumulate extremely high levels of the transition metal vanadium. We previously isolated four vanadium-binding proteins (Vanabins 1–4) and a homologous protein (VanabinP) from the vanadium-rich ascidian Ascidia sydneiensis samea. In the present study, we identified cDNAs encoding five different Vanabin2-related proteins in A. sydneiensis samea blood cells. It was notable that the sequences of the encoded proteins vary from that of Vanabin2 at up to 14 specific positions, while both the polypeptide length and the 18 cysteine residues were completely conserved. The most divergent protein, named 14MT, differed from Vanabin2 at all 14 positions. Using immobilized metal-ion affinity chromatography, we found that Vanabin2 and 14MT have the same metal ion selectivity, but the overall affinity of 14MT for VO2+ is higher than that of Vanabin2. Binding number for VO2+ ions was same between Vanabin2 and 14MT as assessed by gel filtration. These results suggested that sequence variations were under strict evolutionary constraints and high affinity binding sites for VO2+ are conserved among Vanabin2 variants.
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journal title |
Biochimica et Biophysica Acta (BBA) - General Subjects
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volume | Volume 1780
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issue | Issue 7-8
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start page | 1010
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end page | 1015
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date of issued | 2008-07
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publisher | Elsevier Science BV
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issn | 0304-4165
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ncid | |
publisher doi | |
language |
eng
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nii type |
Journal Article
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HU type |
Journal Articles
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DCMI type | text
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format | application/pdf
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text version | author
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rights | Copyright (c) 2008 Elsevier B.V.
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relation url | |
department |
Graduate School of Science
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